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X-ray diffraction
3Å resolution

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative aminotransferase Chains: A, B, C, D, E, F, G
Molecule details ›
Chains: A, B, C, D, E, F, G
Length: 389 amino acids
Theoretical weight: 43.23 KDa
Source organism: Actinomadura melliaura
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: Q0H2X1 (Residues: 1-369; Coverage: 100%)
Gene name: atS13
Sequence domains: DegT/DnrJ/EryC1/StrS aminotransferase family
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand PLP 1 x PLP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: R32
Unit cell:
a: 233.149Å b: 233.149Å c: 460.859Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.188 0.187 0.22
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

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Citations

3 citation in other articles

Loop dynamics of thymidine diphosphate-rhamnose 3'-O-methyltransferase (CalS11), an enzyme in calicheamicin biosynthesis.
Han et al. (2016)
2 more

7 mentions without citation

What method to use for protein-protein docking?
Porter et al. (2019)
6 more